EC |
4.1.3.30 |
Accepted name: |
methylisocitrate lyase |
Reaction: |
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = succinate + pyruvate |
Glossary: |
(2S,3R)-2-methylisocitrate = (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = threo-Ds-2-methylisocitrate |
Other name(s): |
2-methylisocitrate lyase; MICL; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase |
Systematic name: |
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate pyruvate-lyase (succinate-forming) |
Comments: |
The enzyme acts on threo-Ds-2-methylisocitrate, but not on threo-Ds-isocitrate, threo-DL-isocitrate or erythro-Ls-isocitrate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 57827-77-7 |
References: |
1. |
Tabuchi, T. and Satoh, T. Distinction between isocitrate lyase and methylisocitrate lyase in Candida lipolytica. Agric. Biol. Chem. 40 (1976) 1863–1869. |
2. |
Tabuchi, T. and Satoh, T. Purification and properties of methylisocitrate lyase, a key enzyme in propionate metabolism, from Candida lipolytica. Agric. Biol. Chem. 41 (1977) 169–174. |
|
[EC 4.1.3.30 created 1978] |
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|
|
EC
|
4.1.3.31
|
Transferred entry: | 2-methylcitrate synthase. Now EC 2.3.3.5, 2-methylcitrate synthase
|
[EC 4.1.3.31 created 1978, deleted 2002] |
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|
EC |
4.1.3.34 |
Accepted name: |
citryl-CoA lyase |
Reaction: |
(3S)-citryl-CoA = acetyl-CoA + oxaloacetate |
Other name(s): |
(3S)-citryl-CoA oxaloacetate-lyase |
Systematic name: |
(3S)-citryl-CoA oxaloacetate-lyase (acetyl-CoA-forming) |
Comments: |
The enzyme is a component of EC 4.1.3.6 {[citrate (pro-3S)-lyase]}and EC 2.3.3.8 [ATP citrate synthase]. Also acts on (3S)-citryl thioacyl-carrier protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 131095-35-7 |
References: |
1. |
Dimroth, P., Loyal, R. and Eggerer, H. Characterization of the isolated transferase subunit of citrate lyase as a CoA-transferase. Evidence against a covalent enzyme-substrate intermediate. Eur. J. Biochem. 80 (1977) 479–488. [DOI] [PMID: 336371] |
2. |
Lill, U., Schreil, A. and Eggerer, H. Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase. Eur. J. Biochem. 125 (1982) 645–650. [DOI] [PMID: 6749502] |
|
[EC 4.1.3.34 created 1984, modified 1986] |
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|
|
EC |
4.2.1.3 |
Accepted name: |
aconitate hydratase |
Reaction: |
citrate = isocitrate (overall reaction) (1a) citrate = cis-aconitate + H2O (1b) cis-aconitate + H2O = isocitrate |
|
For diagram of the citric acid cycle, click here and for diagram of the glyoxylate cycle, click here |
Glossary: |
isocitrate = (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate (previously known as threo-Ds-isocitrate)
cis-aconitate = (Z)-prop-1-ene-1,2,3-tricarboxylate |
Other name(s): |
cis-aconitase; aconitase; AcnB; 2-methylaconitate hydratase; citrate(isocitrate) hydro-lyase |
Systematic name: |
citrate(isocitrate) hydro-lyase (cis-aconitate-forming) |
Comments: |
Besides interconverting citrate and cis-aconitate, it also interconverts cis-aconitate with isocitrate and, hence, interconverts citrate and isocitrate. The equilibrium mixture is 91% citrate, 6% isocitrate and 3% aconitate. cis-Aconitate is used to designate the isomer (Z)-prop-1-ene-1,2,3-tricarboxylate. An iron-sulfur protein, containing a [4Fe-4S] cluster to which the substrate binds. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9024-25-3 |
References: |
1. |
Dickman, S.R. Aconitase. In: Boyer, P.D., Lardy, H. and Myrbäck, K (Ed.), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 495–510. |
2. |
Morrison, J.F. The purification of aconitase. Biochem. J. 56 (1954) 99–105. [PMID: 13126098] |
3. |
Lauble, H., Kennedy, M.C., Beinert, H. and Stout, C.D. Crystal structures of aconitase with trans-aconitate and nitrocitrate bound. J. Mol. Biol. 237 (1994) 437–451. [DOI] [PMID: 8151704] |
|
[EC 4.2.1.3 created 1961, modified 2003] |
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EC
|
4.2.1.4
|
Deleted entry: | citrate dehydratase. Now known to be a partial reaction catalysed by EC 4.2.1.3, aconitate hydratase. |
[EC 4.2.1.4 created 1961, deleted 2013] |
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|
EC |
4.2.1.36 |
Accepted name: |
homoaconitate hydratase |
Reaction: |
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate = (Z)-but-1-ene-1,2,4-tricarboxylate + H2O |
|
For diagram of l-lysine synthesis, click here |
Glossary: |
cis-homoaconitate = (Z)-but-1-ene-1,2,4-tricarboxylate
(R)-homocitrate = (2R)-2-hydroxybutane-1,2,4-tricarboxylate
homoisocitrate = (-)-threo-homoisocitrate = (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate |
Other name(s): |
homoaconitase; cis-homoaconitase; HACN; Lys4; LysF; 2-hydroxybutane-1,2,4-tricarboxylate hydro-lyase (incorrect) |
Systematic name: |
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate hydro-lyase [(Z)-but-1-ene-1,2,4-tricarboxylate-forming] |
Comments: |
Requires a [4Fe-4S] cluster for activity. The enzyme from the hyperthermophilic eubacterium Thermus thermophilus can catalyse the reaction shown above but cannot catalyse the previously described reaction, i.e. formation of (R)-homocitrate by hydration of cis-homoaconitate. The enzyme responsible for the conversion of cis-homoaconitate into (R)-homocitrate in T. thermophilus is unknown at present but the reaction can be catalysed in vitro using aconitate hydratase from pig (EC 4.2.1.3) [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-68-6 |
References: |
1. |
Strassman, M. and Ceci, L.N. Enzymatic formation of cis-homoaconitic acid, an intermediate in lysine biosynthesis in yeast. J. Biol. Chem. 241 (1966) 5401–5407. [PMID: 5954805] |
2. |
Jia, Y., Tomita, T., Yamauchi, K., Nishiyama, M. and Palmer, D.R. Kinetics and product analysis of the reaction catalysed by recombinant homoaconitase from Thermus thermophilus. Biochem. J. 396 (2006) 479–485. [DOI] [PMID: 16524361] |
3. |
Zabriskie, T.M. and Jackson, M.D. Lysine biosynthesis and metabolism in fungi. Nat. Prod. Rep. 17 (2000) 85–97. [PMID: 10714900] |
|
[EC 4.2.1.36 created 1972, modified 2007] |
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|
EC |
4.2.1.79 |
Accepted name: |
2-methylcitrate dehydratase |
Reaction: |
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H2O |
Glossary: |
(2S,3S)-2-methylcitrate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate
cis-2-methylaconitate = (Z)-but-2-ene-1,2,3-tricarboxylate |
Other name(s): |
2-methylcitrate hydro-lyase; PrpD; 2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase |
Systematic name: |
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase [(Z)-but-2-ene-1,2,3-tricarboxylate-forming] |
Comments: |
The enzyme is specific for (2S,3S)-methylcitrate, showing no activity with (2R,3S)-methylcitrate [2]. The enzyme can also use cis-aconitate as a substrate but more slowly [2]. Both this enzyme and EC 4.2.1.3, aconitate hydratase, are required to complete the isomerization of (2S,3S)-methylcitrate to (2R,3S)-2-methylisocitrate [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 80891-26-5 |
References: |
1. |
Aoki, H. and Tabuchi, T. Purification and properties of 2-methylcitrate dehydratase from Yarrowia lipolytica. Agric. Biol. Chem. 45 (1981) 2831–2837. |
2. |
Brock, M., Maerker, C., Schütz, A., Völker, U. and Buckel, W. Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase. Eur. J. Biochem. 269 (2002) 6184–6194. [DOI] [PMID: 12473114] |
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[EC 4.2.1.79 created 1984] |
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|
EC |
4.2.1.99 |
Accepted name: |
2-methylisocitrate dehydratase |
Reaction: |
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H2O |
Glossary: |
cis-2-methylaconitate = (Z)-but-2-ene-1,2,3-tricarboxylate
(2S,3R)-2-methylisocitrate = (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = threo-Ds-2-methylisocitrate |
Other name(s): |
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase |
Systematic name: |
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase [(Z)-but-2-ene-1,2,3-tricarboxylate-forming] |
Comments: |
The enzyme from the fungus Yarrowia lipolytica (Saccharomycopsis) does not act on isocitrate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 170780-51-5 |
References: |
1. |
Aoki, H., Uchiyama, H., Umetsu, H., Tabuchi, T. Isolation of 2-methylisocitrate dehydratase, a new enzyme serving in the methylcitric acid cycle for propionate metabolism, from Yarrowia lipolytica. Biosci. Biotechnol. Biochem. 59 (1995) 1825–1828. |
2. |
Tabuchi, T., Umetsu, H., Aoki, H., Uchiyama, H. Characteristics of 2-methylisocitrate dehydratase, isolated from Yarrowia lipolytica, in comparison to aconitase. Biosci. Biotechnol. Biochem. 59 (1995) 2013–2017. |
|
[EC 4.2.1.99 created 1999] |
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EC |
4.2.1.114 |
Accepted name: |
methanogen homoaconitase |
Reaction: |
(R)-2-hydroxybutane-1,2,4-tricarboxylate = (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate (overall reaction) (1a) (R)-2-hydroxybutane-1,2,4-tricarboxylate = (Z)-but-1-ene-1,2,4-tricarboxylate + H2O (1b) (Z)-but-1-ene-1,2,4-tricarboxylate + H2O = (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate |
|
For diagram of the 2-aminoadipate pathway of L-lysine synthesis, click here |
Glossary: |
cis-homoaconitate = (Z)-but-1-ene-1,2,4-tricarboxylate
(R)-homocitrate = (R)-2-hydroxybutane-1,2,4-tricarboxylate
homoisocitrate = (–)-threo-homoisocitrate = (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate |
Other name(s): |
methanogen HACN |
Systematic name: |
(R)-2-hydroxybutane-1,2,4-tricarboxylate hydro-lyase [(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate-forming] |
Comments: |
This enzyme catalyses several reactions in the pathway of coenzyme-B biosynthesis in methanogenic archaea. Requires a [4Fe-4S] cluster for activity. In contrast to EC 4.2.1.36, homoaconitate hydratase, this enzyme can catalyse both the dehydration of (R)-homocitrate to form cis-homoaconitate and the subsequent hydration reaction that forms homoisocitrate. In addition to cis-homoaconitate, the enzyme can also catalyse the hydration of the physiological substrates dihomoaconitate and trihomoaconitate as well as the non-physiological substrate tetrahomoaconitate. cis-Aconitate and threo-DL-isocitrate cannot act as substrates, and (S)-homocitrate and trans-homoaconitate act as inhibitors of the enzyme. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Drevland, R.M., Jia, Y., Palmer, D.R. and Graham, D.E. Methanogen homoaconitase catalyzes both hydrolyase reactions in coenzyme B biosynthesis. J. Biol. Chem. 283 (2008) 28888–28896. [DOI] [PMID: 18765671] |
|
[EC 4.2.1.114 created 2009] |
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|
EC |
4.2.1.117 |
Accepted name: |
2-methylcitrate dehydratase (2-methyl-trans-aconitate forming) |
Reaction: |
(2S,3S)-2-methylcitrate = 2-methyl-trans-aconitate + H2O |
Glossary: |
(2S,3S)-2-methylcitrate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate
2-methyl-trans-aconitate = (2E)-but-2-ene-1,2,3-tricarboxylate |
Systematic name: |
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate hydro-lyase (2-methyl-trans-aconitate-forming) |
Comments: |
Catalyses the dehydration of (2S,3S)-2-methylcitrate, forming the trans isomer of 2-methyl-aconitate (unlike EC 4.2.1.79, which forms only the cis isomer). Part of a propionate degradation pathway. The enzyme from Shewanella oneidensis can also accept citrate and cis-aconitate, but activity with (2S,3S)-2-methylcitrate was approximately 2.5-fold higher. 2-methylisocitrate and isocitrate were not substrates [1]. An iron-sulfur protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Grimek, T.L. and Escalante-Semerena, J.C. The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF function in vivo. J. Bacteriol. 186 (2004) 454–462. [DOI] [PMID: 14702315] |
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[EC 4.2.1.117 created 2009] |
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EC |
5.1.2.6 |
Accepted name: |
isocitrate epimerase |
Reaction: |
(1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate = (1S,2S)-1-hydroxypropane-1,2,3-tricarboxylate |
|
For diagram of reaction, click here |
Glossary: |
isocitrate = (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate = threo-Ds-isocitrate
allocitrate = (1S,2S)-1-hydroxypropane-1,2,3-tricarboxylate = D-erythro-isocitrate |
Systematic name: |
(1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate 1-epimerase |
Comments: |
(1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate is the commonly occurring isomer of isocitrate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81210-68-6 |
References: |
1. |
Hoshiko, S., Kunimoto, Y., Arima, K. and Beppu, T. Mechanism of L-alloisocitric acid fermentation: isocitrate epimerase activity in the cell-free-extract of Penicillium purpurogenum. Agric. Biol. Chem. 46 (1982) 143–151. |
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[EC 5.1.2.6 created 1984] |
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EC |
6.2.1.18 |
Accepted name: |
citrate—CoA ligase |
Reaction: |
ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA |
Glossary: |
citrate = 2-hydroxypropane-1,2,3-tricarboxylate |
Other name(s): |
citryl-CoA synthetase; citrate:CoA ligase; citrate thiokinase |
Systematic name: |
citrate:CoA ligase (ADP-forming) |
Comments: |
The enzyme is a component of EC 2.3.3.8 ATP citrate synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 856428-87-0 |
References: |
1. |
Lill, U., Schreil, A. and Eggerer, H. Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase. Eur. J. Biochem. 125 (1982) 645–650. [DOI] [PMID: 6749502] |
2. |
Aoshima, M., Ishii, M. and Igarashi, Y. A novel enzyme, citryl-CoA synthetase, catalysing the first step of the citrate cleavage reaction in Hydrogenobacter thermophilus TK-6. Mol. Microbiol. 52 (2004) 751–761. [DOI] [PMID: 15101981] |
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[EC 6.2.1.18 created 1986] |
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EC |
6.2.1.22 |
Accepted name: |
[citrate (pro-3S)-lyase] ligase |
Reaction: |
ATP + acetate + holo-[citrate (pro-3S)-lyase] = AMP + diphosphate + acetyl-[citrate (pro-3S)-lyase] |
Glossary: |
citrate = 2-hydroxypropane-1,2,3-tricarboxylate |
Other name(s): |
citrate lyase ligase; citrate lyase synthetase; acetate: SH-[acyl-carrier-protein] enzyme ligase (AMP); acetate:HS-citrate lyase ligase; acetate:citrate-(pro-3S)-lyase(thiol-form) ligase (AMP-forming); acetate:[citrate-(pro-3S)-lyase](thiol-form) ligase (AMP-forming) |
Systematic name: |
acetate:holo-[citrate-(pro-3S)-lyase] ligase (AMP-forming) |
Comments: |
Both this enzyme and EC 2.3.1.49,deacetyl-[citrate-(pro-3S)-lyase] S-acetyltransferase, acetylate and activate EC 4.1.3.6, citrate (pro-3S)-lyase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52660-22-7 |
References: |
1. |
Antranikian, G. and Gottschalk, G. Copurification of citrate lyase and citrate lyase ligase from Rhodopseudomonas gelatinosa and subsequent separation of the two enzymes. Eur. J. Biochem. 126 (1982) 43–47. [DOI] [PMID: 7128585] |
2. |
Antranikian, G., Herzberg, C. and Gottschalk, G. Covalent modification of citrate lyase ligase from Clostridium sphenoides by phosphorylation/dephosphorylation. Eur. J. Biochem. 153 (1985) 413–420. [DOI] [PMID: 3935436] |
3. |
Quentmeier, A. and Antranikian, G. Characterization of citrate lyase from Clostridium sporosphaeroides. Arch. Microbiol. 141 (1985) 85–90. [PMID: 3994485] |
4. |
Schmellenkamp, H. and Eggerer, H. Mechanism of enzymic acetylation of des-acetyl citrate lyase. Proc. Natl. Acad. Sci. USA 71 (1974) 1987–1991. [DOI] [PMID: 4365579] |
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[EC 6.2.1.22 created 1989] |
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EC |
6.3.1.17 |
Accepted name: |
β-citrylglutamate synthase |
Reaction: |
ATP + citrate + L-glutamate = ADP + phosphate + β-citryl-L-glutamate |
Other name(s): |
NAAG synthetase I; NAAGS-I; RIMKLB (gene name) (ambiguous) |
Systematic name: |
citrate:L-glutamate ligase (ADP-forming) |
Comments: |
The enzyme, found in animals, also has the activity of EC 6.3.2.41, N-acetylaspartylglutamate synthase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Collard, F., Stroobant, V., Lamosa, P., Kapanda, C.N., Lambert, D.M., Muccioli, G.G., Poupaert, J.H., Opperdoes, F. and Van Schaftingen, E. Molecular identification of N-acetylaspartylglutamate synthase and β-citrylglutamate synthase. J. Biol. Chem. 285 (2010) 29826–29833. [DOI] [PMID: 20657015] |
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[EC 6.3.1.17 created 2014] |
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EC
|
6.3.2.27
|
Deleted entry: | The activity is covered by two independent enzymes, EC 6.3.2.38 N2-citryl-N6-acetyl-N6-hydroxylysine synthase, and EC 6.3.2.39, aerobactin synthase |
[EC 6.3.2.27 created 2002, modified 2006, deleted 2012] |
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|
EC |
6.3.2.38 |
Accepted name: |
N2-citryl-N6-acetyl-N6-hydroxylysine synthase |
Reaction: |
2 ATP + citrate + N6-acetyl-N6-hydroxy-L-lysine + H2O = 2 ADP + 2 phosphate + N6-acetyl-N2-citryl-N6-hydroxy-L-lysine |
|
For diagram of aerobactin biosynthesis, click here |
Glossary: |
citryl = 3-hydroxy-3,4-dicarboxybutanoyl |
Other name(s): |
Nα-citryl-Nε-acetyl-Nε-hydroxylysine synthase; iucA (gene name) |
Systematic name: |
citrate:N6-acetyl-N6-hydroxy-L-lysine ligase (AMP-forming) |
Comments: |
Requires Mg2+. The enzyme is involved in the biosynthesis of aerobactin, a dihydroxamate siderophore. It belongs to a class of siderophore synthases known as type A nonribosomal peptide synthase-independent synthases (NIS). Type A enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate. The enzyme is believed to form an adenylate intermediate prior to ligation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Gibson, F. and Magrath, D.I. The isolation and characterization of a hydroxamic acid (aerobactin) formed by Aerobacter aerogenes 62-I. Biochim. Biophys. Acta 192 (1969) 175–184. [DOI] [PMID: 4313071] |
2. |
Maurer, P.J. and Miller, M. Microbial iron chelators: total synthesis of aerobactin and its constituent amino acid, N6-acetyl-N6-hydroxylysine. J. Am. Chem. Soc. 104 (1982) 3096–3101. |
3. |
de Lorenzo, V., Bindereif, A., Paw, B.H. and Neilands, J.B. Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. J. Bacteriol. 165 (1986) 570–578. [DOI] [PMID: 2935523] |
4. |
Appanna, D.L., Grundy, B.J., Szczepan, E.W. and Viswanatha, T. Aerobactin synthesis in a cell-free system of Aerobacter aerogenes 62-1. Biochim. Biophys. Acta 801 (1984) 437–443. |
5. |
Challis, G.L. A widely distributed bacterial pathway for siderophore biosynthesis
independent of nonribosomal peptide synthetases. ChemBioChem 6 (2005) 601–611. [DOI] [PMID: 15719346] |
6. |
Oves-Costales, D., Kadi, N. and Challis, G.L. The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis. Chem. Commun. (Camb.) (2009) 6530–6541. [PMID: 19865642] |
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[EC 6.3.2.38 created 2012, modified 2019] |
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|
|
EC |
6.3.2.39 |
Accepted name: |
aerobactin synthase |
Reaction: |
ATP + N2-citryl-N6-acetyl-N6-hydroxy-L-lysine + N6-acetyl-N6-hydroxy-L-lysine = AMP + diphosphate + aerobactin |
|
For diagram of aerobactin biosynthesis, click here |
Other name(s): |
iucC (gene name) |
Systematic name: |
N2-citryl-N6-acetyl-N6-hydroxy-L-lysine:N6-acetyl-N6-hydroxy-L-lysine ligase (AMP-forming) |
Comments: |
Requires Mg2+. The enzyme is involved in the biosynthesis of aerobactin, a dihydroxamate siderophore. It belongs to a class of siderophore synthases known as type C nonribosomal peptide synthase-independent synthases (NIS). Type C enzymes are responsible for the formation of amide or ester bonds between a variety of substrates and a prochiral carboxyl group of a citrate molecule that is already linked to a different moiety at its other prochiral carboxyl group. The enzyme is believed to form an adenylate intermediate prior to ligation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Gibson, F. and Magrath, D.I. The isolation and characterization of a hydroxamic acid (aerobactin) formed by Aerobacter aerogenes 62-I. Biochim. Biophys. Acta 192 (1969) 175–184. [DOI] [PMID: 4313071] |
2. |
Maurer, P.J. and Miller, M. Microbial iron chelators: total synthesis of aerobactin and its constituent amino acid, N6-acetyl-N6-hydroxylysine. J. Am. Chem. Soc. 104 (1982) 3096–3101. |
3. |
Appanna, D.L., Grundy, B.J., Szczepan, E.W. and Viswanatha, T. Aerobactin synthesis in a cell-free system of Aerobacter aerogenes 62-1. Biochim. Biophys. Acta 801 (1984) 437–443. |
4. |
de Lorenzo, V., Bindereif, A., Paw, B.H. and Neilands, J.B. Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. J. Bacteriol. 165 (1986) 570–578. [DOI] [PMID: 2935523] |
5. |
de Lorenzo, V. and Neilands, J.B. Characterization of iucA and iucC genes of the aerobactin system of plasmid ColV-K30 in Escherichia coli. J. Bacteriol. 167 (1986) 350–355. [DOI] [PMID: 3087960] |
6. |
Challis, G.L. A widely distributed bacterial pathway for siderophore biosynthesis
independent of nonribosomal peptide synthetases. ChemBioChem 6 (2005) 601–611. [DOI] [PMID: 15719346] |
7. |
Oves-Costales, D., Kadi, N. and Challis, G.L. The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis. Chem. Commun. (Camb.) (2009) 6530–6541. [PMID: 19865642] |
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[EC 6.3.2.39 created 2012, modified 2019] |
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EC |
6.3.2.54 |
Accepted name: |
L-2,3-diaminopropanoate—citrate ligase |
Reaction: |
ATP + L-2,3-diaminopropanoate + citrate = AMP + diphosphate + 2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate |
Glossary: |
staphyloferrin B = 5-[(2-{[(3S)-5-{[(2S)-2-amino-2-carboxyethyl]amino}-3-carboxy-3-hydroxy-5-oxopentanoyl]amino}ethyl)amino]-2,5-dioxopentanoate |
Other name(s): |
sbnE (gene name); 2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate synthtase |
Systematic name: |
L-2,3-diaminopropanoate:citrate ligase (2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate-forming) |
Comments: |
Requires Mg2+. The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B. It belongs to a class of siderophore synthases known as type A nonribosomal peptide synthase-independent synthases (NIS). Type A NIS enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate. The enzyme forms a citrate adenylate intermediate prior to ligation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Dale, S.E., Doherty-Kirby, A., Lajoie, G. and Heinrichs, D.E. Role of siderophore biosynthesis in virulence of Staphylococcus aureus: identification and characterization of genes involved in production of a siderophore. Infect. Immun. 72 (2004) 29–37. [PMID: 14688077] |
2. |
Cheung, J., Beasley, F.C., Liu, S., Lajoie, G.A. and Heinrichs, D.E. Molecular characterization of staphyloferrin B biosynthesis in Staphylococcus aureus. Mol. Microbiol. 74 (2009) 594–608. [PMID: 19775248] |
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[EC 6.3.2.54 created 2019] |
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EC |
6.3.2.57 |
Accepted name: |
staphyloferrin A synthase |
Reaction: |
ATP + N5-[(S)-citryl]-D-ornithine + citrate = AMP + diphosphate + staphyloferrin A |
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For diagram of staphyloferrin A biosynthesis, click here |
Glossary: |
staphyloferrin A = N2-[(R)-citryl],N5-[(S)-citryl]-D-ornithine
citryl = 3-hydroxy-3,4-dicarboxybutanoyl |
Other name(s): |
sfnaB (gene name) |
Systematic name: |
N5-[(S)-citryl]-D-ornithine:citrate ligase (staphyloferrin A-forming) |
Comments: |
Requires Mg2+. The enzyme, characterized from the bacterium Staphylococcus aureus, catalyses the last step in the biosynthesis of the siderophore staphyloferrin A. It belongs to a class of siderophore synthases known as type A nonribosomal peptide synthase-independent synthases (NIS). Type A NIS enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate. The enzyme forms a citrate adenylate intermediate prior to ligation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Cotton, J.L., Tao, J. and Balibar, C.J. Identification and characterization of the Staphylococcus aureus gene cluster coding for staphyloferrin A. Biochemistry 48 (2009) 1025–1035. [PMID: 19138128] |
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[EC 6.3.2.57 created 2019] |
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EC |
6.3.2.58 |
Accepted name: |
D-ornithine—citrate ligase |
Reaction: |
ATP + D-ornithine + citrate = AMP + diphosphate + N5-[(S)-citryl]-D-ornithine |
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For diagram of staphyloferrin A biosynthesis, click here |
Glossary: |
staphyloferrin A = N2-[(R)-citryl],N5-[(S)-citryl]-D-ornithine |
Other name(s): |
sfnaD (gene name) |
Systematic name: |
D-ornithine:citrate ligase {3-[(2-aminopentan-5-oylcarbamoyl)methyl]-3-hydroxybutanoate-forming} |
Comments: |
Requires Mg2+. The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin A. It belongs to a class of siderophore synthases known as type A nonribosomal peptide synthase-independent synthases (NIS). Type A NIS enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate. The enzyme forms a citrate adenylate intermediate prior to ligation. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Cotton, J.L., Tao, J. and Balibar, C.J. Identification and characterization of the Staphylococcus aureus gene cluster coding for staphyloferrin A. Biochemistry 48 (2009) 1025–1035. [PMID: 19138128] |
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[EC 6.3.2.58 created 2019] |
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EC |
6.4.1.7 |
Accepted name: |
2-oxoglutarate carboxylase |
Reaction: |
ATP + 2-oxoglutarate + HCO3- = ADP + phosphate + oxalosuccinate |
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For diagram of reaction, click here |
Glossary: |
oxalosuccinate = 1-oxopropane-1,2,3-tricarboxylate |
Other name(s): |
oxalosuccinate synthetase; carboxylating factor for ICDH (incorrect); CFI; OGC |
Comments: |
A biotin-containing enzyme that requires Mg2+ for activity. It was originally thought [1] that this enzyme was a promoting factor for the carboxylation of 2-oxoglutarate by EC 1.1.1.41, isocitrate dehydrogenase (NAD+), but this has since been disproved [2]. The product of the reaction is unstable and is quickly converted into isocitrate by the action of EC 1.1.1.41 [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60382-75-4 |
References: |
1. |
Aoshima, M., Ishii, M. and Igarashi, Y. A novel biotin protein required for reductive carboxylation of 2-oxoglutarate by isocitrate dehydrogenase in Hydrogenobacter thermophilus TK-6. Mol. Microbiol. 51 (2004) 791–798. [DOI] [PMID: 14731279] |
2. |
Aoshima, M. and Igarashi, Y. A novel oxalosuccinate-forming enzyme involved in the reductive carboxylation of 2-oxoglutarate in Hydrogenobacter thermophilus TK-6. Mol. Microbiol. 62 (2006) 748–759. [DOI] [PMID: 17076668] |
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[EC 6.4.1.7 created 2006] |
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EC |
7.2.2.18 |
Accepted name: |
ABC-type ferric citrate transporter |
Reaction: |
ATP + H2O + Fe3+-dicitrate-[dicitrate-binding protein][side 1] = ADP + phosphate + Fe3+-dicitrate[side 2] + [dicitrate-binding protein][side 1] |
Other name(s): |
ferric citrate transporting ATPase; ferric citrate ABC transporter; fecBCDE (gene names) |
Systematic name: |
ATP phosphohydrolase (ABC-type, iron(III) dicitrate-importing) |
Comments: |
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from Escherichia coli interacts with a periplasmic substrate binding protein and mediates the high affinity uptake of Fe3+-citrate in the form of a mononuclear (containing one iron(III) ion and two citrate molecules) or dinuclear (containing 2 iron(III) ions) complexes. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Staudenmaier, H., Van Hove, B., Yaraghi, Z. and Braun, V. Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli. J. Bacteriol. 171 (1989) 2626–2633. [PMID: 2651410] |
2. |
Banerjee, S., Paul, S., Nguyen, L.T., Chu, B.C. and Vogel, H.J. FecB, a periplasmic ferric-citrate transporter from E. coli, can bind different forms of ferric-citrate as well as a wide variety of metal-free and metal-loaded tricarboxylic acids. Metallomics 8 (2016) 125–133. [PMID: 26600288] |
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[EC 7.2.2.18 created 2000 as EC 3.6.3.34, part transferred 2018 to EC 7.2.2.18] |
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